Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00114
Entry Name
UniProt Accession
Theoretical PI
5.83
Molecular Weight
21768.13
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Transforming protein RhoA
Protein Synonyms/Alias
Rho cDNA clone 12; h12;
Gene Name
RHOA
Gene Synonyms/Alias
ARH12; ARHA; RHO12;
Created Date
01-JAN-1988
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
159
Canonical
GAFGYMECSAKTKDG
[1]
S-Palmitoylation
190
Canonical
RGKKKSGCLVL****
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Predicted from GPS-Lipid
Functional Description
Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Plays an essential role in cleavage furrow formation. Required for the apical junction formation of keratinocyte cell-cell adhesion. Serves as a target for the yopT cysteine peptidase from Yersinia pestis, vector of the plague, and Yersinia pseudotuberculosis, which causes gastrointestinal disorders. Stimulates PKN2 kinase activity. May be an activator of PLCE1. Activated by ARHGEF2, which promotes the exchange of GDP for GTP. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. The MEMO1-RHOA- DIAPH1 signaling pathway plays an important role in ERBB2- dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization.
Sequence Annotation
Nucleotide-binding: 12 19 GTP.
Nucleotide-binding: 59 63 GTP.
Nucleotide-binding: 117 120 GTP.
Motif: 34 42 Effector region.
Functional site: 189 190 Cleavage; by yopT.
Modified residue: 34 34 O-AMP-tyrosine; by Haemophilus IbpA.
Modified residue: 37 37 O-AMP-threonine; by Vibrio VopS.
Modified residue: 41 41 ADP-ribosylasparagine; by botulinumtoxin.
Modified residue: 188 188 Phosphoserine; by PKG/PRKG1.
Modified residue: 190 190 Cysteine methyl ester.
Protein Length
193 AA.
Protein Sequence
(Canonical)
MAAIRKKLVI VGDGACGKTC LLIVFSKDQF PEVYVPTVFE NYVADIEVDG KQVELALWDT  60
AGQEDYDRLR PLSYPDTDVI LMCFSIDSPD SLENIPEKWT PEVKHFCPNV PIILVGNKKD  120
LRNDEHTRRE LAKMKQEPVK PEEGRDMANR IGAFGYMECS AKTKDGVREV FEMATRAALQ  180
ARRGKKKSGC LVL                                                     193
FASTA
(Canonical)
>LipidDB-9606-00114|P61586
MAAIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYVADIEVDGKQVELALWDT
AGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKD
LRNDEHTRRELAKMKQEPVKPEEGRDMANRIGAFGYMECSAKTKDGVREVFEMATRAALQ
ARRGKKKSGCLVL
Gene Ontology
GO:0043296; C:apical junction complex; IDA:UniProtKB
GO:0030424; C:axon; IEA:Ensembl
GO:0005938; C:cell cortex; IDA:UniProtKB
GO:0030054; C:cell junction; TAS:Reactome
GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW
GO:0005829; C:cytosol; TAS:Reactome
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0005925; C:focal adhesion; IDA:UniProtKB
GO:0030027; C:lamellipodium; ISS:UniProtKB
GO:0005739; C:mitochondrion; IEA:Ensembl
GO:0005634; C:nucleus; IEA:Ensembl
GO:0005886; C:plasma membrane; TAS:Reactome
GO:0032587; C:ruffle membrane; IEA:Ensembl
GO:0019003; F:GDP binding; IEA:Ensembl
GO:0005525; F:GTP binding; IEA:UniProtKB-KW
GO:0003924; F:GTPase activity; TAS:UniProtKB
GO:0017022; F:myosin binding; IPI:UniProtKB
GO:0030036; P:actin cytoskeleton organization; TAS:UniProtKB
GO:0030521; P:androgen receptor signaling pathway; IEA:Ensembl
GO:0043297; P:apical junction assembly; IMP:UniProtKB
GO:0038027; P:apolipoprotein A-I-mediated signaling pathway; IMP:UniProtKB
GO:0007411; P:axon guidance; TAS:Reactome
GO:0007596; P:blood coagulation; TAS:Reactome
GO:0007160; P:cell-matrix adhesion; IEA:Ensembl
GO:0021795; P:cerebral cortex cell migration; IEA:Ensembl
GO:0036089; P:cleavage furrow formation; IDA:UniProtKB
GO:0021861; P:forebrain radial glial cell differentiation; IEA:Ensembl
GO:0050919; P:negative chemotaxis; IMP:UniProtKB
GO:0050771; P:negative regulation of axonogenesis; TAS:Reactome
GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl
GO:0033144; P:negative regulation of intracellular steroid hormone receptor signaling pathway; IEA:Ensembl
GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl
GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl
GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome
GO:0043931; P:ossification involved in bone maturation; ISS:BHF-UCL
GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome
GO:0030168; P:platelet activation; TAS:Reactome
GO:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl
GO:0050772; P:positive regulation of axonogenesis; TAS:Reactome
GO:0045785; P:positive regulation of cell adhesion; IEA:Ensembl
GO:0030307; P:positive regulation of cell growth; IEA:Ensembl
GO:0030335; P:positive regulation of cell migration; IEA:Ensembl
GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl
GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB
GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEP:UniProtKB
GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl
GO:0045666; P:positive regulation of neuron differentiation; IMP:MGI
GO:0042346; P:positive regulation of NF-kappaB import into nucleus; NAS:UniProtKB
GO:0071803; P:positive regulation of podosome assembly; IEA:Ensembl
GO:0045987; P:positive regulation of smooth muscle contraction; IEA:Ensembl
GO:0051496; P:positive regulation of stress fiber assembly; IDA:MGI
GO:0045727; P:positive regulation of translation; IEA:Ensembl
GO:0045907; P:positive regulation of vasoconstriction; IEA:Ensembl
GO:0050770; P:regulation of axonogenesis; TAS:Reactome
GO:0051924; P:regulation of calcium ion transport; IEA:Ensembl
GO:0030334; P:regulation of cell migration; IMP:UniProtKB
GO:0050773; P:regulation of dendrite development; IEA:Ensembl
GO:2000177; P:regulation of neural precursor cell proliferation; IEA:Ensembl
GO:0033688; P:regulation of osteoblast proliferation; ISS:BHF-UCL
GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome
GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IEA:Ensembl
GO:0043200; P:response to amino acid; IEA:Ensembl
GO:0042493; P:response to drug; IEA:Ensembl
GO:0045471; P:response to ethanol; IEA:Ensembl
GO:0051384; P:response to glucocorticoid; IEA:Ensembl
GO:0009749; P:response to glucose; IEA:Ensembl
GO:0001666; P:response to hypoxia; IEA:Ensembl
GO:0009612; P:response to mechanical stimulus; IEA:Ensembl
GO:0007266; P:Rho protein signal transduction; TAS:UniProtKB
GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl
GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome
GO:0090307; P:spindle assembly involved in mitosis; IMP:BHF-UCL
GO:0043149; P:stress fiber assembly; IEA:Ensembl
GO:0031098; P:stress-activated protein kinase signaling cascade; IEA:Ensembl
GO:0021762; P:substantia nigra development; IEP:UniProt
GO:0061383; P:trabecula morphogenesis; ISS:BHF-UCL
GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome
GO:0016032; P:viral process; IEA:UniProtKB-KW
Interpro
InterPro; IPR027417; P-loop_NTPase
InterPro; IPR005225; Small_GTP-bd_dom
InterPro; IPR001806; Small_GTPase
InterPro; IPR003578; Small_GTPase_Rho
Pfam
Pfam; PF00071; Ras;
SMART
SMART; SM00174; RHO;
PROSITE
PROSITE; PS51420; RHO;
PRINTS
PRINTS; PR00449; RASTRNSFRMNG;